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Key Documents

103241

Sigma-Aldrich

4-Methoxy-1-naphthaldehyde

99%

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About This Item

Formule linéaire :
CH3OC10H6CHO
Numéro CAS:
Poids moléculaire :
186.21
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352100
ID de substance PubChem :
Nomenclature NACRES :
NA.22

Pureté

99%

Forme

solid

Point d'ébullition

212 °C/40 mmHg (lit.)

Pf

35-36 °C (lit.)

Chaîne SMILES 

COc1ccc(C=O)c2ccccc12

InChI

1S/C12H10O2/c1-14-12-7-6-9(8-13)10-4-2-3-5-11(10)12/h2-8H,1H3

Clé InChI

MVXMNHYVCLMLDD-UHFFFAOYSA-N

Application

4-Methoxy-1-naphthaldehyde was used in fluorometric enzymatic assay for determination of activity of class I and II alcohol dehydrogenase isoenzymes in human pancreas and in human liver homogenates.

Actions biochimiques/physiologiques

4-Methoxy-1-naphthaldehyde is fluorogenic substrate for human alcohol dehydrogenase (ADH).

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


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Consulter la Bibliothèque de documents

Jayaraman Jayabharathi et al.
Journal of fluorescence, 26(1), 307-316 (2015-11-21)
Efficient hole transport materials based on novel fused methoxynaphthyl phenanthrimidazole core structure were synthesised and characterized. Their device performances in phosphorescent organic light emitting diodes were investigated. The high thermal stability in combination with the reversible oxidation process made promising
L Chrostek et al.
Clinical chemistry and laboratory medicine, 38(5), 409-412 (2000-08-22)
We have measured the activity of class I and II alcohol dehydrogenase isoenzymes in the sera of patients with liver tumours, using class-specific fluorogenic naphthaldehydes as substrates. The activity of the tested isoenzymes was unchanged in primary tumours and significantly
Lech Chrostek et al.
Journal of clinical laboratory analysis, 17(3), 93-96 (2003-04-16)
Alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH), which are most abundant in the liver, are the main enzymes involved in ethanol metabolism in humans. Gender-related differences in total liver ADH and ALDH activity among different animal species have been observed
J Wierzchowski et al.
Analytical chemistry, 64(2), 181-186 (1992-01-15)
Both class I and class II alcohol dehydrogenase (ADH) activities are present in human serum. The contribution of each class can be measured using two class-specific, fluorogenic substrates, 4-methoxy-1-naphthaldehyde and 6-methoxy-2-naphthaldehyde. The former is highly selective for class I isozymes
Lech Chrostek et al.
Digestive diseases and sciences, 48(7), 1230-1233 (2003-07-23)
Ethanol metabolism in the pancreas occurs predominantly by way of an nonoxidative pathway to fatty acid ethyl esters but oxidative routes to acetaldehyde also may contribute to injury of pancreatic cells. Three metabolic systems are responsible for the oxidative metabolism

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